TY - JOUR AU - el Battioui, Kamal AU - Chakraborty, Sohini AU - Wacha, András AU - Molnár, Dániel AU - Quemé-Peña, Mayra AU - Szigyártó, Imola Cs. AU - Szabó, Csenge Lilla AU - Bodor, Andrea AU - Horváti, Kata AU - Gyulai, Gergő AU - Bősze, Szilvia AU - Mihály, Judith AU - Jezsó, Bálint AU - Románszki, Loránd AU - Tóth, Judit AU - Varga, Zoltán AU - Mándity, István AU - Juhász, Tünde AU - Beke-Somfai, Tamás TI - In situ captured antibacterial action of membrane-incising peptide lamellae JF - NATURE COMMUNICATIONS J2 - NAT COMMUN VL - 15 PY - 2024 IS - 1 PG - 14 SN - 2041-1723 DO - 10.1038/s41467-024-47708-4 UR - https://m2.mtmt.hu/api/publication/34819821 ID - 34819821 AB - Developing unique mechanisms of action are essential to combat the growing issue of antimicrobial resistance. Supramolecular assemblies combining the improved biostability of non-natural compounds with the complex membrane-attacking mechanisms of natural peptides are promising alternatives to conventional antibiotics. However, for such compounds the direct visual insight on antibacterial action is still lacking. Here we employ a design strategy focusing on an inducible assembly mechanism and utilized electron microscopy (EM) to follow the formation of supramolecular structures of lysine-rich heterochiral β 3 -peptides, termed lamellin-2K and lamellin-3K, triggered by bacterial cell surface lipopolysaccharides. Combined molecular dynamics simulations, EM and bacterial assays confirmed that the phosphate-induced conformational change on these lamellins led to the formation of striped lamellae capable of incising the cell envelope of Gram-negative bacteria thereby exerting antibacterial activity. Our findings also provide a mechanistic link for membrane-targeting agents depicting the antibiotic mechanism derived from the in-situ formation of active supramolecules. LA - English DB - MTMT ER - TY - JOUR AU - Csomos, Attila AU - Madarász, Miklós AU - Turczel, Gábor AU - Cseri, Levente AU - Bodor, Andrea AU - Anett, Matuscsák AU - Katona, Gergely AU - Kovács, Ervin AU - Rózsa J., Balázs AU - Mucsi, Zoltán TI - A GFP inspired 8-methoxyquinoline-derived fluorescent molecular sensor for the detection of Zn2+ by two-photon microscopy JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J PY - 2024 SN - 0947-6539 DO - 10.1002/chem.202400009 UR - https://m2.mtmt.hu/api/publication/34724516 ID - 34724516 AB - An effective, GFP-inspired fluorescent Zn2+ sensor is developed for two-photon microscopy and related biological application that featured an 8-methoxyquinoline moiety. Excellent photophysical characteristics including a 37-fold fluorescence enhancement with excitation and emission maxima at 440 nm and 505 nm, respectively, as well as a high two-photon cross-section of 73 GM at 880 nm are reported. Based on the experimental data, the relationship between the structure and properties was elucidated and explained backed up by DFT calculations, particularly to the observed PeT phenomenon for the turn-on process. Biological validation and detailed experimental and theoretical characterization of the free and the zinc-bound compounds are presented. LA - English DB - MTMT ER - TY - CONF AU - Sebák, Fanni AU - Szabó, Csenge Lilla AU - Ecsédi, Péter AU - Burkhard, LUY AU - Nyitray, László AU - Bodor, Andrea ED - Majdik, Cornelia TI - A rendezetlen fehérjék és az NMR spektroszkópia T2 - XXIX. Nemzetközi Vegyészkonferencia / 29th International Conference on Chemistry PB - Erdélyi Magyar Műszaki Tudományos Társaság (EMT) C1 - Kolozsvár T3 - Nemzetközi Vegyészkonferencia, ISSN 1843-6293 PY - 2023 SP - 1 PG - 1 UR - https://m2.mtmt.hu/api/publication/34236962 ID - 34236962 LA - English DB - MTMT ER - TY - JOUR AU - Sebák, Fanni AU - Ecsédi, Péter AU - Nyitray, László AU - Bodor, Andrea TI - Assignment of the disordered, proline-rich N-terminal domain of the tumour suppressor p53 protein using 1HN and 1Hα-detected NMR measurements JF - BIOMOLECULAR NMR ASSIGNMENTS J2 - BIOMOL NMR ASSIGM VL - 17 PY - 2023 IS - 2 SP - 309 EP - 314 PG - 6 SN - 1874-2718 DO - 10.1007/s12104-023-10160-4 UR - https://m2.mtmt.hu/api/publication/34213192 ID - 34213192 N1 - Analytical and BioNMR Laboratory, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter sétány 1/a, Budapest, 1117, Hungary Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, Budapest, 1117, Hungary Export Date: 15 November 2023 Correspondence Address: Bodor, A.; Analytical and BioNMR Laboratory, Pázmány Péter sétány 1/a, Hungary; email: andrea.bodor@ttk.elte.hu AB - Protein p53 is mostly known for playing a key role in tumour suppression, and mutations in the p53 gene are amongst the most frequent genomic events accompanying oncogenic transformation. Continuous research is conducted to target disordered proteins/protein regions for cancer therapy, for which atomic level information is also necessary. The disordered N-terminal part of p53 contains the transactivation and the proline-rich domains—which besides being abundant in proline residues—contains repetitive Pro-Ala motifs. NMR assignment of such repetitive, proline-rich regions is challenging due to the lack of amide protons in the 1 H N -detected approaches, as well as due to the small chemical shift dispersion. In the present study we perform the full assignment of the p53 1–100 region by applying a combination of 1 H N - and 1 H α -detected NMR experiments. We also show the increased information content when using real-time homo- and heteronuclear decoupled acquisition schemes. On the other hand, we highlight the presence of minor proline species, and using Pro-selective experiments we determine the corresponding cis or trans conformation. Secondary chemical shifts for (C α –C β ) atoms indicate the disordered nature of this region, with expected helical tendency for the TAD1 region. As the role of the proline-rich domain is yet not well understood our results can contribute to further successful investigations. LA - English DB - MTMT ER - TY - JOUR AU - Sebák, Fanni AU - Szolomájer, János AU - Papp, Nándor AU - Tóth, Gábor AU - Bodor, Andrea TI - Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides JF - FRONTIERS IN BIOSCIENCE-LANDMARK J2 - FRONT BIOSCI-LANDMARK VL - 28 PY - 2023 IS - 6 PG - 8 SN - 2768-6701 DO - 10.31083/j.fbl2806127 UR - https://m2.mtmt.hu/api/publication/34043118 ID - 34043118 N1 - Analytical and BioNMR Laboratory, Institute of Chemistry, Eötvös Loránd University, Budapest, 1117, Hungary Department of Medical Chemistry, University of Szeged, Szeged, 6720, Hungary Hevesy György PhD School of Chemistry, Eötvös Loránd University, Budapest, 1117, Hungary Export Date: 28 July 2023 Correspondence Address: Bodor, A.; Analytical and BioNMR Laboratory, Hungary; email: andrea.bodor@ttk.elte.hu Chemicals/CAS: proline, 147-85-3, 7005-20-1; Intrinsically Disordered Proteins; Peptides; Proline LA - English DB - MTMT ER - TY - JOUR AU - Kovács, Dániel AU - Bodor, Andrea TI - The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs JF - RSC ADVANCES J2 - RSC ADV VL - 13 PY - 2023 IS - 15 SP - 10182 EP - 10203 PG - 22 SN - 2046-2069 DO - 10.1039/D3RA00977G UR - https://m2.mtmt.hu/api/publication/33729542 ID - 33729542 AB - In studying secondary structural propensities of proteins by nuclear magnetic resonance (NMR) spectroscopy, secondary chemical shifts (SCSs) are the primary atomic scale observables. But which random coil chemical shift (RCCS) values to choose? LA - English DB - MTMT ER - TY - THES AU - Bodor, Andrea TI - Az NMR spektroszkópia sokszínűsége fehérjék és kismolekulák világában PY - 2022 UR - https://m2.mtmt.hu/api/publication/34396850 ID - 34396850 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Beke-Somfai, Tamas AU - El, Battioui Kamal AU - Juhasz, Tunde AU - Queme-Pena, Mayra AU - Szigyarto, Imola AU - Molnar, Daniel AU - Toth, Judit AU - Szabo, Lilla AU - Bodor, Andrea AU - Wacha, András Ferenc AU - Mandity, Istvan TI - Conformational diversity of membrane active beta[sup]3[/sup]-peptide foldamers JF - JOURNAL OF PEPTIDE SCIENCE J2 - J PEPT SCI VL - 28 PY - 2022 IS - 3 PG - 2 SN - 1075-2617 UR - https://m2.mtmt.hu/api/publication/34034694 ID - 34034694 N1 - Funding Agency and Grant Number: Hungarian Academy of Sciences [LP2016-2]; National Competitiveness and Excellence Program [NVKP_16-1-2016-0007]; GINOP grant [BIONANO_GINOP-2.3.2-15-2016-00017] Funding text: This work was funded by the Momentum Programme (LP2016-2) of the Hungarian Academy of Sciences, the National Competitiveness and Excellence Program (NVKP_16-1-2016-0007) and the GINOP grant (BIONANO_GINOP-2.3.2-15-2016-00017). Supplement: 3 LA - English DB - MTMT ER - TY - JOUR AU - Haller, Jens D. AU - Bodor, Andrea AU - Luy, Burkhard TI - Pure shift amide detection in conventional and TROSY-type experiments of 13C,15N-labeled proteins JF - JOURNAL OF BIOMOLECULAR NMR J2 - J BIOMOL NMR VL - 76 PY - 2022 IS - 5-6 SP - 213 EP - 221 PG - 9 SN - 0925-2738 DO - 10.1007/s10858-022-00406-z UR - https://m2.mtmt.hu/api/publication/33258560 ID - 33258560 N1 - Institute of Organic Chemistry and Institute for Biological Interfaces 4 – Magnetic Resonance, Karlsruhe Institute of Technology (KIT), Hermann-Von-Helmholtz-Platz 1, Eggenstein-Leopoldshafen, 76344, Germany Institute of Chemistry, Analytical and BioNMR Laboratory, ELTE –Eötvös Loránd University, Pázmány Péter Sétány 1/A, Budapest, 1117, Hungary Export Date: 2 December 2022 CODEN: JBNME Correspondence Address: Haller, J.D.; Institute of Organic Chemistry and Institute for Biological Interfaces 4 – Magnetic Resonance, Hermann-Von-Helmholtz-Platz 1, Germany; email: jens.haller@kit.edu AB - Large coupling networks in uniformly 13 C, 15 N-labeled biomolecules induce broad multiplets that even in flexible proteins are frequently not recognized as such. The reason is that given multiplets typically consist of a large number of individual resonances that result in a single broad line, in which individual components are no longer resolved. We here introduce a real-time pure shift acquisition scheme for the detection of amide protons which is based on 13 C-BIRD r,X . As a result the full homo- and heteronuclear coupling network can be suppressed at low power leading to real singlets at substantially improved resolution and uncompromised sensitivity. The method is tested on a small globular and an intrinsically disordered protein (IDP) where the average spectral resolution is increased by a factor of ~ 2 and higher. Equally important, the approach works without saturation of water magnetization for solvent suppression and exchanging amide protons are not affected by saturation transfer. LA - English DB - MTMT ER - TY - JOUR AU - Szabó, Csenge Lilla AU - Szabó, Beáta AU - Sebák, Fanni AU - Bermel, Wolfgang AU - Tantos, Ágnes AU - Bodor, Andrea TI - The Disordered EZH2 Loop: Atomic Level Characterization by 1HN- and 1Hα-Detected NMR Approaches, Interaction with the Long Noncoding HOTAIR RNA JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 23 PY - 2022 IS - 11 SN - 1661-6596 DO - 10.3390/ijms23116150 UR - https://m2.mtmt.hu/api/publication/32853030 ID - 32853030 N1 - Analytical and BioNMR Laboratory, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter Sétány 1/A, Budapest, 1117, Hungary Hevesy György Ph.D. School of Chemistry, Eötvös Loránd University, Pázmány Péter Sétány 1/A, Budapest, 1117, Hungary Institute of Enzymology, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, Budapest, 1117, Hungary Bruker BioSpin GmbH, Rudolf-Plank Str. 23, Ettlingen, 76275, Germany Export Date: 24 October 2022 Correspondence Address: Tantos, A.; Institute of Enzymology, Magyar Tudósok Körútja 2, Hungary; email: tantos.agnes@ttk.hu Chemicals/CAS: proline, 147-85-3, 7005-20-1; serine, 56-45-1, 6898-95-9; threonine, 36676-50-3, 72-19-5; Enhancer of Zeste Homolog 2 Protein; RNA, Long Noncoding LA - English DB - MTMT ER -